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biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
brenda
strain CGMCC2428
-
-
brenda
strain CGMCC2428
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
strain YJ-407, gene pmi1
UniProt
brenda
strain YJ-407, gene pmi1
UniProt
brenda
enzyme from Bacillus subtilis strain HB002; ATCC 23857
UniProt
brenda
-
-
-
brenda
different cultivars, gene pmi
-
-
brenda
cultivar Suzhouqing
UniProt
brenda
strain J2315, bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
brenda
type II enzyme, bifunctional protein with phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
SwissProt
brenda
Cassia coluteoides
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
Microorganisms
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
strain PAO1. Bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
brenda
DSM 3638
-
-
brenda
bifunctional enzyme with mannose-6-phosphate isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
brenda
bifunctional enzyme with mannose-6-phosphate isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
brenda
-
-
-
brenda
strain DJ77, gene pmi
-
-
brenda
strain DJ77, gene pmi
-
-
brenda
-
-
-
brenda
-
-
-
brenda
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
isoform Pmi1; isoform Pmi2
-
-
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
-
-
-
brenda
wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli
-
-
brenda
-
2818, 2829, 3354, 660706, 661902, 663077, 663078, 663079, 663166, 702663, 716883, 727158, 728469
-
-
brenda
expression in Brassica rapa
-
-
brenda
expression in Linum usitatissimum
-
-
brenda
expression in Malus domestica
-
-
brenda
expression in onion
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase
-
-
brenda
strain PAO1. Bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
brenda
bifunctional phosphoglucose isomerase/phosphomannose isomerase, EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
brenda
bifunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.8 and EC 5.3.1.9, overexpression in Escherichia coli
-
-
brenda
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
-
-
brenda
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
brenda
-
2624, 2806, 2807, 2811, 2816, 2817, 2828, 652637, 661119, 662318, 702663
-
-
brenda
secretory mutant with a thermolabile phosphomannose isomerase
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction

uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
malfunction
-
the manA-deficient mutant is unable to utilize D-mannose as a sole carbon source
malfunction
-
uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
-
malfunction
-
the manA-deficient mutant is unable to utilize D-mannose as a sole carbon source
-
metabolism

-
the enzyme is part of the biosynthetic pathway of sugar nucleotides essential for welan gum production in Alcaligenes sp., overview
metabolism
-
phosphomannose isomerase catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate in the extracellular polysaccharide synthesis pathway, feedback regulation of this pathway
metabolism
the enzyme catalyzes the first committed step in the synthesis of mannose-containing sugar chains and provides a link between glucose metabolism and mannosylation
metabolism
-
the enzyme is part of the biosynthetic pathway of sugar nucleotides essential for welan gum production in Alcaligenes sp., overview
-
metabolism
-
the enzyme catalyzes the first committed step in the synthesis of mannose-containing sugar chains and provides a link between glucose metabolism and mannosylation
-
metabolism
-
phosphomannose isomerase catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate in the extracellular polysaccharide synthesis pathway, feedback regulation of this pathway
-
physiological function

-
phosphomannose isomerase has a major effect on the formation of a complete, branched extracellular polysaccharide. The manA gene influences biofilm maturation but not initial attachment
physiological function
isoform PMI2 overexpression in tobacco can increase tolerance to oxidative stress
physiological function
-
phosphomannose isomerase has a major effect on the formation of a complete, branched extracellular polysaccharide. The manA gene influences biofilm maturation but not initial attachment
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-D-fructose 6-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
r
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
D-fructose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
D-mannose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
D-Mannose 6-phosphate
D-Fructose 6-phosphate
D-ribose 5-phosphate
D-ribulose 5-phosphate
additional information
?
-
beta-D-mannose 6-phosphate

beta-D-fructose 6-phosphate
-
-
-
-
r
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
-
-
-
-
r
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
-
-
-
?
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
-
-
-
-
?
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
-
-
-
?
D-Allose

D-Psicose
-
-
-
r
D-Allose
D-Psicose
-
-
-
-
r
D-Allose
D-Psicose
-
-
-
-
r
D-Fructose 6-phosphate

?
-
enzyme is involved in alginate biosynthesis
-
-
-
D-Fructose 6-phosphate
?
-
-
-
-
-
D-Fructose 6-phosphate
?
-
first enzyme of the N-glycosylation pathway
-
-
-
D-Fructose 6-phosphate
?
Microorganisms
-
mannose 6-phosphate produced in this manner can be incorporated via mannose 1-phosphate as intermediate into guanosine diphosphomannose which participates in numerous processes related to cell wall biosynthesis
-
-
-
D-fructose 6-phosphate

D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate

D-mannose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
r
D-glucose 6-phosphate

D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-Lyxose

D-Xylulose
-
-
-
r
D-Lyxose
D-Xylulose
-
38% conversion yield after 3 h
-
-
?
D-Lyxose
D-Xylulose
-
-
-
-
r
D-Lyxose
D-Xylulose
-
-
-
-
r
D-Mannose

D-Fructose
-
-
-
r
D-Mannose
D-Fructose
-
-
-
-
r
D-Mannose 6-phosphate

?
Cassia coluteoides
-
enzyme is involved in the utilization of mannose released by hydrolysis of galactomannan on germination after phosphorylation to mannose 6-phosphate
-
-
-
D-Mannose 6-phosphate
?
-
channeling D-mannose 6-phosphate into glycolysis by isomerization to fructose 6-phosphate
-
-
-
D-Mannose 6-phosphate

D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
Cassia coluteoides
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
Microorganisms
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
beta-D-fructose 6-phosphate serves as substrate in the reverse direction
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
highly specific for the beta anomer of mannose 6-phosphate, the alpha anomer has no activity as a substrate, and is, at best, a poor inhibitor
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
best substrate
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
best substrate
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
-
D-Ribose

D-Ribulose
-
-
-
r
D-Ribose
D-Ribulose
-
-
-
-
r
D-Ribose
D-Ribulose
-
-
-
-
r
D-ribose 5-phosphate

D-ribulose 5-phosphate
very low activity
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
very low activity
-
-
r
D-talose

D-tagatose
-
-
-
r
D-talose
D-tagatose
-
-
-
-
r
L-allose

L-psicose
-
-
-
r
L-allose
L-psicose
-
-
-
-
r
L-Lyxose

L-Xylulose
-
-
-
r
L-Lyxose
L-Xylulose
-
-
-
-
r
L-Lyxose
L-Xylulose
-
-
-
-
r
L-Mannose

L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-ribose

L-ribulose
-
-
-
r
L-ribose
L-ribulose
-
29% conversion yield after 3 h
-
-
?
L-ribose
L-ribulose
-
-
-
-
r
L-ribulose

L-ribose
best substrate
-
-
r
L-ribulose
L-ribose
-
highest activity
-
-
r
L-talose

L-tagatose
-
-
-
r
L-talose
L-tagatose
-
-
-
-
r
additional information

?
-
-
the enzyme is specific for aldose substrates possessing hydroxyl groups oriented in the same direction at the C-2 and C-3 positions, such as the D- and L-enantiomers of ribose, lyxose, talose, mannose, and allose, substrate specificity, overview
-
-
-
additional information
?
-
the enzyme is specific for aldose substrates possessing hydroxyl groups oriented in the same direction at the C-2 and C-3 positions, such as the D- and L-enantiomers of ribose, lyxose, talose, mannose, and allose, substrate specificity, overview
-
-
-
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
-
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
-
additional information
?
-
-
reversible isomerization of mannose 6-phosphate and fructose 6-phosphate is the initial commited step in the synthesis of the mannosylated glycoproteins, which are essential in biosynthesis of functional fungal cell wall. Absence of mannose-6-phosphate isomerase causes cell lysis
-
-
-
additional information
?
-
-
Molecular mechanics study of enzyme substrate and inhibitors, overview
-
-
-
additional information
?
-
-
enzyme substrate specificity with diverse monosaccharide aldoses and ketoses, overview
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
critical role in the supply of the D-mannose derivatives required for many glycosylation reactions
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
adaptive enzyme
-
-
-
additional information
?
-
-
Molecular mechanics study of enzyme substrate and inhibitors, overview
-
-
-
additional information
?
-
-
PMI is bifunctional possessing both mannose 6-phosphate isomerase and GDP-mannose diphosphorylase activities
-
-
-
additional information
?
-
-
PMI is bifunctional possessing both mannose 6-phosphate isomerase and GDP-mannose diphosphorylase activities
-
-
-
additional information
?
-
no activity with D-glucose 6-phosphate and arabinose 5-phosphate
-
-
-
additional information
?
-
no activity with D-glucose 6-phosphate and arabinose 5-phosphate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+

activates
Ca2+
best activator, may be replaced by Mg2+ or Mn2+ for phosphomannose isomerase activity
Ca2+
2 mM, maximum activity
Ca2+
the enzyme is not stimulated by Ca2+
Co2+

-
can reverse inhibition by a metal binding agent
Co2+
activates, best metal ion, maximal activity at 0.5 mM
Co2+
-
activates, best activator metal ion
Co2+
strong stimulation of activity
Co2+
-
required for phosphomannose isomerase activity
Co2+
2 mM, about 80% of the activity with Cu2+
Co2+
-
can reverse inhibition by EDTA
Co2+
-
beste metal ion activator
Co2+
-
about 230% activity at 0.5 mM
Cu2+

activates
Cu2+
significantly stimulated by Cu2+
Cu2+
-
maximal activity of the recombinant enzyme for L-ribulose isomerization in the presence of 0.5 mM Cu2+
Cu2+
about 135% activity at 0.5 mM
Fe2+

-
can reverse inhibition by a metal binding agent
Fe2+
-
can reverse inhibition by EDTA
Fe2+
about 125% activity at 0.5 mM
Mg2+

activates
Mg2+
60% of activity with Ca2+ for phosphomannose isomerase activity
Mg2+
best activating divalent metal ion
Mg2+
-
activates only the GMP activity of the enzyme
Mg2+
about 175% activity at 0.5 mM
Mn2+

-
can reverse inhibition by a metal binding agent
Mn2+
65% of activity with Ca2+ for phosphomannose isomerase activity
Mn2+
significantly stimulated by Mn2+
Mn2+
2 mM, about 55% of the activity with Cu2+
Mn2+
-
about 160% activity at 0.5 mM
Mn2+
about 175% activity at 0.5 mM
Ni2+

activates
Zinc

-
enzyme contains an essential zinc atom. Four of the five ligands come from the protein, one of these ligands is unique in that it is a glutamine
Zinc
-
recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins
Zinc
-
recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins
Zinc
-
contains 1 gatom per mol of enzyme
Zn2+

-
at low concentrations complete reactivation of enzyme inhibited by a metal binding agent
Zn2+
-
noncovalent complexation, ESI-FTICR study, binding/release of metal ion changes substrate binding affinity by at least 5fold
Zn2+
-
zinc-dependent metalloenzyme
Zn2+
-
zinc-dependent metalloenzyme
Zn2+
-
can reverse inhibition by EDTA
Zn2+
enzyme-bound, Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site
Zn2+
-
about 130% activity at 0.5 mM
Zn2+
Zn2+ is present at one molecule per monomer, the enzyme has about 240% activity in the presence of 0.5 mM Zn2+
additional information

-
mannose-6-phosphate isomerases are metalloenzymes that require a divalent ion metal cofactor for activity and catalysis
additional information
mannose-6-phosphate isomerases are metalloenzymes that require a divalent ion metal cofactor for activity and catalysis
additional information
-
the enzyme requires divalent cations for activity
additional information
-
activated by bivalent cations in the order: Co2+, Ni2+, Mn2+, Mg2+, Ca2+, Zn2+
additional information
absolute requirement for divalent cation
additional information
divalent cations are absolutely required for activity, metal binding increases the thermostability of the enzyme
additional information
-
PMI absolutely requires divalent metal cations for catalytic activity
additional information
-
the enzyme is not affected by Ca2+, Mg2+, Ba2+, and Ni2+
additional information
-
activated by bivalent cations in decreasing order: Co2+, Zn2+, Mn2+, Ni2+, Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,3-Butanedione
-
inactivation
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone
5-deoxy-5-malonyl-D-arabinonohydroxamic acid
-
-
5-deoxy-5-phosphonomethyl-D-arabinonate
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
5-phospho-D-arabinonhydrazide
5-phospho-D-arabinonohydroxamic acid
6-deoxy-6-carboxymethyl-D-mannose
6-deoxy-6-dicarboxymethyl-D-mannose
6-deoxy-6-dimethylmalonate-D-mannopyranose
6-deoxy-6-phosphonomethyl-D-mannose
6-phospho-2-deoxygluconate
Cassia coluteoides
-
competitive
6-Phosphomannonate
Cassia coluteoides
-
competitive
ADP-glucose
-
0.5 mM, 77.8% of initial activity
Ag+
-
irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme
alpha-D-mannose 6-phosphate
-
poor
Ba2+
about 30% inhibition at 0.5 mM
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose
D-mannose 1-phosphate
-
0.5 mM, 81.9% of initial activity
Fe2+
-
12% residual activity at 0.5 mM
fructose 1-phosphate
-
competitive
Galactose 6-hosphate
-
competitive
-
GDP-D-mannose
-
inhibits mannose 6-phosphate isomerase activity of PMI, feedback regulation of this pathway
GDP-mannose
-
0.5 mM, 46.7% of initial activity
glucosamine 6-phosphate
-
competitive
glucose 1-phosphate
-
competitive
glucose 6-phosphate
-
competitive
L-ascorbic acid
-
1 mM, 77% residual activity
N,2,3,4,5-pentahydroxypentanamide
-
-
p-chloromercuribenzoate
-
0.05 mM, 33% residual activity; 0.05 mM, 39% residual activity
ribose 5-phosphate
-
competitive
S-nitroso-acetyl-penicillamine
-
dose- and time-dependent inactivation
sorbitol 6-phosphate
-
competitive
1,10-phenanthroline

-
-
2,2'-dipyridyl

-
-
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone

-
-
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone
-
-
5-deoxy-5-phosphonomethyl-D-arabinonate

-
-
5-deoxy-5-phosphonomethyl-D-arabinonate
-
-
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide

-
-
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
-
-
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid

-
-
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
-
-
5-phospho-D-arabinonhydrazide

-
-
5-phospho-D-arabinonhydrazide
-
; in 50 mM HEPES buffer, pH 7.1, at 25°C
5-phospho-D-arabinonohydroxamic acid

-
nanomolar inhibitor
5-phospho-D-arabinonohydroxamic acid
-
-
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25°C; nanomolar inhibitor
5-phospho-D-arabinonohydroxamic acid
-
50% inhibition at 0.000169 mM, inhibition of both type I and type II isozymes
5-phospho-D-arabinonohydroxamic acid
-
50% inhibition at 0.000136 mM, inhibition of both type I and type II isozymes
6-deoxy-6-carboxymethyl-D-mannose

-
-
6-deoxy-6-carboxymethyl-D-mannose
-
-
6-deoxy-6-dicarboxymethyl-D-mannose

-
-
6-deoxy-6-dicarboxymethyl-D-mannose
-
-
6-deoxy-6-dimethylmalonate-D-mannopyranose

-
-
6-deoxy-6-dimethylmalonate-D-mannopyranose
-
-
6-deoxy-6-phosphonomethyl-D-mannose

-
-
6-deoxy-6-phosphonomethyl-D-mannose
-
-
6-phosphogluconate

-
6-phosphogluconate
Cassia coluteoides
-
slight inhibition
6-phosphogluconate
-
competitive
arabinose 5-phosphate

-
-
arabinose 5-phosphate
-
-
arabinose 5-phosphate
-
-
arabinose 5-phosphate
-
-
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside

-
-
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
-
-
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose

-
-
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose
-
-
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose

-
-
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose
-
-
Cd2+

-
1 mM, no residual activity
Cd2+
-
competitive, strongly pH dependent
dithiothreitol

-
1 mM, 73% residual activity; 1 mM, 84% residual activity
EDTA

-
-
EDTA
-
2.5 mM, 54% residual activity; 2.5 mM, 86% residual activity
EDTA
complete inactivation
EDTA
2 mM, complete inhibition
EDTA
0.1 mM, about 50% inhibition
EDTA
complete inhibition at 1 mM, reversible by the addition of divalent metal cations such as Zn2+, Mn2+, Co2+, Mg2+ and Ni2+
EDTA
-
about 75% residual activity at 0.5 mM
EDTA
complete inhibition at 0.5 mM
erythrose 4-phosphate

-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
Cassia coluteoides
-
D-erythrose 4-phosphate, competitive
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
; competitive
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
Hg2+

-
partial noncompetitive inhibition with mannose 6-phosphate as substrate. In addition to the inhibition at rapid equilibrium, inactivation occurs in a two-step process, proceeding via an intermediate complex. The rate of the irreversible inactivation can be slowed by the addition of the substrate mannose 6-phosphate
Hg2+
-
recombinant wild-type enzyme and selenomethionine-labelled enzyme
Hg2+
-
competitive, relatively pH-independent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion
mannitol 1-phosphate

Cassia coluteoides
-
competitive
mannitol 1-phosphate
-
competitive
Silver sulfadiazine

-
wild-type enzyme is inhibited, mutant enzyme Cys150Ala is not inhibited
Silver sulfadiazine
-
no inhibition
Zn2+

-
1 mM, no residual activity
Zn2+
-
inhibitory to both phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
Zn2+
-
competitive with mannose 6-phosphate, strongly pH-dependent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion
additional information

-
not inhibitory: mannose 1-phosphate, GTP, GDP-mannose, or diphosphate
-
additional information
not inhibitory: mannose 1-phosphate, GTP, GDP-mannose, or diphosphate
-
additional information
-
synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive enzyme inhibitors. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview
-
additional information
-
not inhibitory: 5-phospho-D-arabinonate
-
additional information
-
no inhibition by N-acetyl-penicillamine
-
additional information
-
not inhibitory: 5-phospho-D-arabinonate
-
additional information
-
synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive inhibitors of the enzyme. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview
-
additional information
-
no inhibition by GTP, mannose 1-phosphate, and phosphodiphosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00043 - 0.33
beta-D-mannose 6-phosphate
0.06 - 0.44
D-fructose 6-phosphate
0.72 - 3.5
D-glucose 6-phosphate
433
D-Lyxose
pH 7.5, 40°C, recombinant enzyme
946
D-mannose
pH 7.5, 40°C, recombinant enzyme
0.0413 - 243
D-mannose 6-phosphate
110
D-ribose
pH 7.5, 40°C, recombinant enzyme
469
D-talose
pH 7.5, 40°C, recombinant enzyme
312
L-allose
pH 7.5, 40°C, recombinant enzyme
998
L-ribose
pH 7.5, 40°C, recombinant enzyme
0.17 - 4
mannose 6-phosphate
additional information
additional information
-
enzyme kinetics with D-lyxose and L-ribose, overview
-
0.00043
beta-D-mannose 6-phosphate

-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.0986
beta-D-mannose 6-phosphate
pH 7.6, 65°C
0.33
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.06
D-fructose 6-phosphate

-
pH 7.4, 80°C
0.15
D-fructose 6-phosphate
-
22°C, pH 7.4
0.2
D-fructose 6-phosphate
80°C, pH 7.4
0.21
D-fructose 6-phosphate
50°C, pH 7.4
0.22
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
0.3
D-fructose 6-phosphate
-
pH 7.4, 50°C
0.44
D-fructose 6-phosphate
80°C, pH 7.4
0.72
D-glucose 6-phosphate

80°C, pH 7.4
3.5
D-glucose 6-phosphate
80°C, pH 7.4
0.0413
D-mannose 6-phosphate

-
pH 7.5, 25°C
0.06
D-mannose 6-phosphate
-
pH 7.4, 80°C
0.121
D-mannose 6-phosphate
-
pH 7.1, 25°C
0.18
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C; mutant enzyme E67A, pH 7.0, 80°C
0.21
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
0.25
D-mannose 6-phosphate
80°C, pH 7.4
0.27
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
0.33
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
0.354
D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.372
D-mannose 6-phosphate
-
pH 7.5, 25°C
0.53
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
0.85
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
1.1
D-mannose 6-phosphate
80°C, pH 7.4
1.18
D-mannose 6-phosphate
-
wild-type, pH 7.0, 25°C
1.21
D-mannose 6-phosphate
-
22°C, pH 7.4
1.29
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
2.5
D-mannose 6-phosphate
-
pH 7.1, 25°C
8 - 9
D-mannose 6-phosphate
mutant enzyme N90A/L129F, at pH 7.0 and 70°C
9
D-mannose 6-phosphate
pH 7.6, presence of 5 mM Mg2+
9.04
D-mannose 6-phosphate
-
mutant E410A, pH 7.0, 25°C
12.28
D-mannose 6-phosphate
-
mutant R479A, pH 7.0, 25°C
12.36
D-mannose 6-phosphate
-
mutant E458A, pH 7.0, 25°C
12.4
D-mannose 6-phosphate
-
30°C, pH 7.6
12.9
D-mannose 6-phosphate
-
mutant N433A, pH 7.0, 25°C
15.9
D-mannose 6-phosphate
-
mutant R373A, pH 7.0, 25°C
16.26
D-mannose 6-phosphate
-
mutant H411A, pH 7.0, 25°C
23.12
D-mannose 6-phosphate
-
mutant R472A, pH 7.0, 25°C
100
D-mannose 6-phosphate
mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C
149
D-mannose 6-phosphate
wild type enzyme, at pH 7.0 and 70°C
243
D-mannose 6-phosphate
mutant enzyme L129F, at pH 7.0 and 70°C
136
L-ribulose

-
wild type enzyme, at pH 7.0 and 75°C
140
L-ribulose
-
mutant enzyme R142N, at pH 7.0 and 75°C
150
L-ribulose
-
mutant enzyme R142Q, at pH 7.0 and 75°C
151
L-ribulose
-
mutant enzyme R142E, at pH 7.0 and 75°C
184
L-ribulose
-
mutant enzyme R142A, at pH 7.0 and 75°C
228
L-ribulose
-
mutant enzyme R142K, at pH 7.0 and 75°C
308
L-ribulose
-
mutant enzyme R142Y, at pH 7.0 and 75°C
0.17
mannose 6-phosphate

-
-
0.2
mannose 6-phosphate
-
Hepes buffer
0.23
mannose 6-phosphate
-
recombinant enzyme
0.25
mannose 6-phosphate
-
wild-type enzyme
0.65
mannose 6-phosphate
-
-
0.73
mannose 6-phosphate
-
-
0.8
mannose 6-phosphate
-
selenomethionine-labelled enzyme, Hepes buffer
1
mannose 6-phosphate
-
Tris/HCl buffer
1.24
mannose 6-phosphate
-
-
1.35
mannose 6-phosphate
-
-
1.6
mannose 6-phosphate
Cassia coluteoides
-
enzyme from developing seeds
1.9
mannose 6-phosphate
Cassia coluteoides
-
enzyme from germinating seeds
2
mannose 6-phosphate
-
-
3.03
mannose 6-phosphate
-
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase
4
mannose 6-phosphate
-
selenomethionine-labelled enzyme, Tris/HCl buffer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3 - 23
beta-D-mannose 6-phosphate
141
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
7089
D-Lyxose
pH 7.5, 40°C, recombinant enzyme
3748
D-mannose
pH 7.5, 40°C, recombinant enzyme
0.076 - 112100
D-mannose 6-phosphate
72
D-ribose
pH 7.5, 40°C, recombinant enzyme
63970
D-talose
pH 7.5, 40°C, recombinant enzyme
920
L-allose
pH 7.5, 40°C, recombinant enzyme
17600
L-ribose
pH 7.5, 40°C, recombinant enzyme
121 - 162
mannose 6-phosphate
3 - 6
beta-D-mannose 6-phosphate

-
in 50 mM HEPES buffer, pH 7.1, at 25°C
23
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.076
D-mannose 6-phosphate

-
pH 7.1, 25°C
0.25
D-mannose 6-phosphate
-
mutant R472A, pH 7.0, 25°C
0.54
D-mannose 6-phosphate
-
mutant R479A, pH 7.0, 25°C
0.75
D-mannose 6-phosphate
-
mutant R373A, pH 7.0, 25°C
1.38
D-mannose 6-phosphate
-
wild-type, pH 7.0, 25°C
2.63
D-mannose 6-phosphate
-
mutant E410A, pH 7.0, 25°C
3.25
D-mannose 6-phosphate
-
mutant E458A, pH 7.0, 25°C
3.5
D-mannose 6-phosphate
-
mutant N433A, pH 7.0, 25°C
4.41
D-mannose 6-phosphate
-
mutant H411A, pH 7.0, 25°C
11
D-mannose 6-phosphate
mutant enzyme W13A, pH 7.0, 80°C
19
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C
19.4
D-mannose 6-phosphate
pH 7.6, presence of 5 mM Mg2+
20
D-mannose 6-phosphate
-
pH 7.1, 25°C
31
D-mannose 6-phosphate
mutant enzyme E67A, pH 7.0, 80°C
37
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
54
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
70
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
75
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
1371
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
23550
D-mannose 6-phosphate
wild type enzyme, at pH 7.0 and 70°C
55120
D-mannose 6-phosphate
mutant enzyme L129F, at pH 7.0 and 70°C
85720
D-mannose 6-phosphate
mutant enzyme N90A/L129F, at pH 7.0 and 70°C
112100
D-mannose 6-phosphate
mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C
32670
L-ribulose

-
mutant enzyme R142E, at pH 7.0 and 75°C
48300
L-ribulose
-
mutant enzyme R142Q, at pH 7.0 and 75°C
50640
L-ribulose
-
wild type enzyme, at pH 7.0 and 75°C
56180
L-ribulose
-
mutant enzyme R142Y, at pH 7.0 and 75°C
64870
L-ribulose
-
mutant enzyme R142A, at pH 7.0 and 75°C
68880
L-ribulose
-
mutant enzyme R142K, at pH 7.0 and 75°C
81060
L-ribulose
-
mutant enzyme R142N, at pH 7.0 and 75°C
121
mannose 6-phosphate

-
selenomethionine-labelled enzyme
162
mannose 6-phosphate
-
wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70 - 840
beta-D-mannose 6-phosphate
641
D-fructose 6-phosphate
wild type enzyme, pH 7.0, 80°C
16.4
D-Lyxose
pH 7.5, 40°C, recombinant enzyme
3.5
D-mannose
pH 7.5, 40°C, recombinant enzyme
13 - 6685
D-mannose 6-phosphate
0.6
D-ribose
pH 7.5, 40°C, recombinant enzyme
6.8
D-talose
pH 7.5, 40°C, recombinant enzyme
2.9
L-allose
pH 7.5, 40°C, recombinant enzyme
17.6
L-ribose
pH 7.5, 40°C, recombinant enzyme
70
beta-D-mannose 6-phosphate

-
in 50 mM HEPES buffer, pH 7.1, at 25°C
840
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
13
D-mannose 6-phosphate

mutant enzyme W13A, pH 7.0, 80°C
54
D-mannose 6-phosphate
mutant enzyme R142A, pH 7.0, 80°C
69
D-mannose 6-phosphate
mutant enzyme Q48A, pH 7.0, 80°C
109
D-mannose 6-phosphate
mutant enzyme E132A, pH 7.0, 80°C
158
D-mannose 6-phosphate
wild type enzyme, at pH 7.0 and 70°C
166
D-mannose 6-phosphate
mutant enzyme H50A, pH 7.0, 80°C
174
D-mannose 6-phosphate
mutant enzyme E67A, pH 7.0, 80°C
227
D-mannose 6-phosphate
mutant enzyme L129F, at pH 7.0 and 70°C
278
D-mannose 6-phosphate
mutant enzyme H122A, pH 7.0, 80°C
965
D-mannose 6-phosphate
mutant enzyme N90A/L129F, at pH 7.0 and 70°C
1120
D-mannose 6-phosphate
mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C
6685
D-mannose 6-phosphate
wild type enzyme, pH 7.0, 80°C
182
L-ribulose

-
mutant enzyme R142Y, at pH 7.0 and 75°C
216
L-ribulose
-
mutant enzyme R142E, at pH 7.0 and 75°C
302
L-ribulose
-
mutant enzyme R142K, at pH 7.0 and 75°C
322
L-ribulose
-
mutant enzyme R142Q, at pH 7.0 and 75°C
353
L-ribulose
-
mutant enzyme R142A, at pH 7.0 and 75°C
374
L-ribulose
-
wild type enzyme, at pH 7.0 and 75°C
579
L-ribulose
-
mutant enzyme R142N, at pH 7.0 and 75°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.162
5-deoxy-5-malonyl-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.0006 - 0.002
5-phospho-D-arabinonhydrazide
0.000041 - 0.0008
5-phospho-D-arabinonohydroxamic acid
0.0105 - 0.115
6-deoxy-6-dicarboxymethyl-D-mannose
0.11 - 58
6-phosphogluconate
0.035 - 0.164
erythrose 4-phosphate
0.0014
erythrose-4-phosphate
-
pH 7.4, 50°C
10
N,2,3,4,5-pentahydroxypentanamide
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.0006
5-phospho-D-arabinonhydrazide

-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.002
5-phospho-D-arabinonhydrazide
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.000041
5-phospho-D-arabinonohydroxamic acid

-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.00008
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.000086
5-phospho-D-arabinonohydroxamic acid
-
pH 7.1, 25°C
0.000137
5-phospho-D-arabinonohydroxamic acid
-
pH 7.1, 25°C
0.0008
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.0105
6-deoxy-6-dicarboxymethyl-D-mannose

-
pH 7.1, 25°C, recombinant enzyme
0.115
6-deoxy-6-dicarboxymethyl-D-mannose
-
pH 7.1, 25°C, recombinant enzyme
0.11
6-phosphogluconate

-
pH 7.4, 50°C
2 - 10
6-phosphogluconate
80°C, pH 7.4
58
6-phosphogluconate
80°C, pH 7.4
0.035
erythrose 4-phosphate

80°C, pH 7.4
0.164
erythrose 4-phosphate
80°C, pH 7.4
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3
5-deoxy-5-phosphonomethyl-D-arabinonate
Escherichia coli
-
above, pH 7.1, 25°C, recombinant enzyme
3
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
Escherichia coli
-
above, pH 7.1, 25°C, recombinant enzyme
0.37 - 2.2
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
0.9 - 4.6
6-deoxy-6-carboxymethyl-D-mannose
0.0181 - 0.199
6-deoxy-6-dicarboxymethyl-D-mannose
1.61 - 4.7
6-deoxy-6-phosphonomethyl-D-mannose
0.37
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid

Escherichia coli
-
pH 7.1, 25°C, recombinant enzyme
2.2
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
Saccharomyces cerevisiae
-
pH 7.1, 25°C, recombinant enzyme
0.9
6-deoxy-6-carboxymethyl-D-mannose

Saccharomyces cerevisiae
-
pH 7.1, 25°C, recombinant enzyme
4.6
6-deoxy-6-carboxymethyl-D-mannose
Escherichia coli
-
pH 7.1, 25°C, recombinant enzyme
0.0181
6-deoxy-6-dicarboxymethyl-D-mannose

Saccharomyces cerevisiae
-
pH 7.1, 25°C, recombinant enzyme
0.199
6-deoxy-6-dicarboxymethyl-D-mannose
Escherichia coli
-
pH 7.1, 25°C, recombinant enzyme
1.61
6-deoxy-6-phosphonomethyl-D-mannose

Saccharomyces cerevisiae
-
pH 7.1, 25°C, recombinant enzyme
4.7
6-deoxy-6-phosphonomethyl-D-mannose
Escherichia coli
-
pH 7.1, 25°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.01
wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80°C
0.0101
recombinant enzyme
0.0165
recombinant enzyme
0.0225
recombinant enzyme
0.0659
recombinant enzyme
0.0918
recombinant enzyme
0.269
-
enzyme activity in cells after 54 h growth on maltose
0.3
mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
0.306
-
enzyme activity in cells after 54 h growth on sucrose
0.313
-
enzyme activity in cells after 54 h growth on glucose
0.6
mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
0.74
wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80°C
1.4
mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
1.5
mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
1.7
mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
1.9
mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
2.1
mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
2.8
mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
3 - 8
mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
3
-
wild type enzyme, using D-psicose as substrate, at pH 7.0 and 75°C
4.5
wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80°C
11
mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
19
-
wild type enzyme, using L-mannose as substrate, at pH 7.0 and 75°C
22
-
wild type enzyme, using L-xylulose as substrate, at pH 7.0 and 75°C
23
-
wild type enzyme, using L-lyxose as substrate, at pH 7.0 and 75°C
31
mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
39
mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
40
mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
42
-
wild type enzyme, using L-psicose as substrate, at pH 7.0 and 75°C
44
mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
51
mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
57
-
wild type enzyme, using L-fructose as substrate, at pH 7.0 and 75°C
63
-
wild type enzyme, using L-talose as substrate, at pH 7.0 and 75°C
85
-
wild type enzyme, using D-tagatose as substrate, at pH 7.0 and 75°C
126
-
wild type enzyme, using D-ribulose as substrate, at pH 7.0 and 75°C
128
-
wild type enzyme, using D-xylulose as substrate, at pH 7.0 and 75°C
165
-
wild type enzyme, using D-allose as substrate, at pH 7.0 and 75°C
167
-
wild type enzyme, using D-fructose as substrate, at pH 7.0 and 75°C
194
mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
333
-
wild type enzyme, using D-lyxose as substrate, at pH 7.0 and 75°C
425
-
wild type enzyme, using L-ribose as substrate, at pH 7.0 and 75°C
474
-
mutant enzyme K37A, using L-ribulose as substrate, at pH 7.0 and 75°C
742
-
wild type enzyme, using L-allose as substrate, at pH 7.0 and 75°C
838
-
mutant enzyme W13A, using L-ribulose as substrate, at pH 7.0 and 75°C
842
-
wild type enzyme, using D-mannose as substrate, at pH 7.0 and 75°C
890
-
purified recombinant enzyme
972
-
mutant enzyme D138A, using L-ribulose as substrate, at pH 7.0 and 75°C
1011
-
mutant enzyme K65A, using L-ribulose as substrate, at pH 7.0 and 75°C
1016
-
mutant enzyme Q48A, using L-ribulose as substrate, at pH 7.0 and 75°C
1045
-
mutant enzyme R142E, using L-ribulose as substrate, at pH 7.0 and 75°C
1046
-
mutant enzyme W69A, using L-ribulose as substrate, at pH 7.0 and 75°C
1065
-
mutant enzyme L39A, using L-ribulose as substrate, at pH 7.0 and 75°C
1076
-
mutant enzyme L124A, using L-ribulose as substrate, at pH 7.0 and 75°C
1092
-
mutant enzyme R142Y, using L-ribulose as substrate, at pH 7.0 and 75°C
1194
-
mutant enzyme L18A, using L-ribulose as substrate, at pH 7.0 and 75°C
1214
-
mutant enzyme R142K, using L-ribulose as substrate, at pH 7.0 and 75°C
1270
-
mutant enzyme R142Q, using L-ribulose as substrate, at pH 7.0 and 75°C
1482
-
mutant enzyme R11A, using L-ribulose as substrate, at pH 7.0 and 75°C
1493
-
wild type enzyme, using L-ribulose as substrate, at pH 7.0 and 75°C
1619
-
wild type enzyme, using D-talose as substrate, at pH 7.0 and 75°C
1791
-
mutant enzyme R142A, using L-ribulose as substrate, at pH 7.0 and 75°C
2152
-
mutant enzyme R14N, using L-ribulose as substrate, at pH 7.0 and 75°C
16

-
wild type enzyme, using L-tagatose as substrate, at pH 7.0 and 75°C
16
mutant enzyme K37A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
58

-
wild type enzyme, using D-ribose as substrate, at pH 7.0 and 75°C
58
mutant enzyme L18A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
75

-
-
75
wild type enzyme, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C
additional information

-
substrate specificity, overview
additional information
substrate specificity, overview
additional information
-
-
additional information
-
mass spectrometry based method for the direct determination of kinetic konstants of enzyme
additional information
-
-
additional information
-
enzyme activity and metabolic parameters in different tissue at different reproductive stages in female and male animals, PMI shows no variability, overview
additional information
-
-
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33548
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
35000
2 * 35000, SDS-PAGE, 2 * 35150, calculated
35150
2 * 35000, SDS-PAGE, 2 * 35150, calculated
36100
2 * 36000, SDS-PAGE, 2 * 36100, calculated
36444
* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation
36452
-
1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 36452, sequence calculation
36500
* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation
36600
gel filtration, recombinant enzyme
46520
-
calculation from nucleotide sequence encoded by cDNA
46530
-
recombinant enzyme, electrospray mass spectroscopy
48740
-
wild-type recombinant enzyme, electrospray mass spectroscopy
49060
-
selenomethionine-labelled enzyme expressed in E. coli, electrospray mass spectroscopy
50000
-
x * 50000, recombinant His6-tagged enzyme, SDS-PAGE
52900
x * 52900, SDS-PAGE
55000
x * 55300, calculated, x * 55000, SDS-PAGE
55300
x * 55300, calculated, x * 55000, SDS-PAGE
55716
-
x * 55716, calculated, x * 56000, SDS-PAGE
61000
-
x * 61000, calculation from nucleotide sequence
65000
-
sedimentation equilibrium, analytical ultracentrifugation
68000
Cassia coluteoides
-
enzyme from pods, gel filtration
74500
Cassia coluteoides
-
enzyme from pods and seeds, density gradient centrifugation
29000

-
gel filtration
29000
1 * 29000, SDS-PAGE
29054

-
1 * 29054, calculated from amino acid sequence
29054
1 * 29054, calculated from amino acid sequence
36000

-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
36000
2 * 36000, SDS-PAGE, 2 * 36100, calculated
36000
-
gel filtration, recombinant enzyme
45000

-
gel filtration
54000

-
gel filtration
54000
-
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase, gel filtration
56000

-
x * 56000, SDS-PAGE
56000
-
1 * 56000, bifunctional enzyme: phosphomannose isomerase-guanosine 5-diphospho-D-mannose pyrophosphorylase, SDS-PAGE
56000
-
x * 55716, calculated, x * 56000, SDS-PAGE
67000

Cassia coluteoides
-
enzyme from seeds, gel filtration
67000
analytical ultracentrifugation
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?

-
x * 55716, calculated, x * 56000, SDS-PAGE
?
x * 55300, calculated, x * 55000, SDS-PAGE
?
-
x * 55300, calculated, x * 55000, SDS-PAGE
-
?
-
x * 61000, calculation from nucleotide sequence
?
-
x * 52900, SDS-PAGE
-
?
-
x * 52900, SDS-PAGE
-
?
-
x * 50000, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 50000, recombinant His6-tagged enzyme, SDS-PAGE
-
dimer

2 * 36000, SDS-PAGE, 2 * 36100, calculated
dimer
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
dimer
2 * 35000, SDS-PAGE, 2 * 35150, calculated
monomer

* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation
monomer
-
1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 36452, sequence calculation
monomer
-
1 * 56000, bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE; 1 * 29054, calculated from amino acid sequence
monomer
-
1 * 29000, SDS-PAGE; 1 * 29000, SDS-PAGE; 1 * 29054, calculated from amino acid sequence; 1 * 29054, calculated from amino acid sequence
-
monomer
-
1 * 58000, SDS-PAGE
additional information

-
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is composed of two independent enzymatic domains. The carboxyl terminus is critical for mannose-6-phosphate isomerase
additional information
mannose-6-phosphate isomerase activity is abolished by deletion of the C-terminal 14 residues. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure
additional information
-
mannose-6-phosphate isomerase activity is abolished by deletion of the C-terminal 14 residues. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure
-
additional information
-
mannose-6-phosphate isomerase activity is abolished by deletion of the C-terminal 14 residues. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure
-
additional information
-
PMI possesses two domains with three conserved motifs: a GMP domain at the N-terminus and a PMI domain at the C-terminus
additional information
-
PMI possesses two domains with three conserved motifs: a GMP domain at the N-terminus and a PMI domain at the C-terminus
-
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25
purified recombinant enzyme, half-life is 461 h
28
-
half-life in absence of Zn2+: 110 min, half-life in presence of 0.0002 mM ZnCl2: 270 min
30
purified recombinant enzyme, half-life is 325 h
35
purified recombinant enzyme, half-life is 236 h
37
-
6 min, wild-type enzyme stable, mutant enzyme loses about 90% of activity
50
purified recombinant enzyme, half-life is 10 h
55
-
pH 6.5, 10 min, about 75% loss of native enzyme
60
-
enzyme half-life is 388 h
64 - 85
the half-lives of the enzyme at 65, 70, 75, 80, and 85°C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively
65
-
enzyme half-life is 73 h
65 - 85
-
the enzyme shows half-lives of 22, 10, 5.5, 2.1, and 0.3 h at 65, 70, 75, 80, and 85°C, respectively
70
-
enzyme half-life is 27 h
100
-
melting temperature for thermal unfolding, 60 min, 50% residual activity
40

-
pH 10, about 25% loss of activity; pH 5.5, 1 h, about 35% loss of activity; pH 6.0-9.5, 1 h, no loss of activity
40
purified recombinant enzyme, half-life is 111 h
45

-
pH 6.5, 30 min, native enzyme stable
45
purified recombinant enzyme, half-life is 56 h
additional information

-
first-order kinetics for thermal inactivation
additional information
first-order kinetics for thermal inactivation
additional information
-
thermal inactivation of GTMpi follows first-order kinetics
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Agrobacterium-based expression in Linum usitatissimum
-
cDNA under the control of the GAL1 promoter, expression in Saccharomyces cerevisiae and in Escherichia coli
-
expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain
-
expressed in Escherichia coli ER2566 cells
expressed in Escherichia coli GI724 cells
-
expressed in Nicotiana tabacum transformed with Agrobacterium tumefaciens
expressed in Oryza sativa ssp. japonica varieties Wanjing97 and Nipponbare
-
expression in Agrobacterium tumefaciens
expression in Brassica rapa
-
expression in Escherichia coli
expression in Escherichia coli strain ER2566
expression in Escherichia coli strain ER2566, coexpression with L-arabinose isomerase
-
expression in Pseudomonas aeruginosa
-
gene pmi, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
high level expression in Escherichia coli M15 as inclusion bodies
overexpressed under the control of the tac promoter in the broad-host-range controlled-expression vector pMMB22, expression in Escherichia coli
-
overexpression in both mucoid and nonmucoid strains of Pseudomonas aeruginosa
-
overexpression of the N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
use of enzyme as selectable marker
-
wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli
-
-

-
expressed in Escherichia coli ER2566 cells

-
expressed in Escherichia coli ER2566 cells
expression in Escherichia coli

-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli strain ER2566

expression in Escherichia coli strain ER2566
-
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C150A
-
mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition
L129F
the activity of the mutant is 204% of the activity of the wild type enzyme
L129W
the activity of the mutant is 10% of the activity of the wild type enzyme
L129Y
the activity of the mutant is 94% of the activity of the wild type enzyme
N90A/L129F
the activity of the mutant is about 6fold higher than the activity of the wild type enzyme
W17Q/N90A/L129F
the specific activity and catalytic efficiency for L-ribulose isomerization of this variant are 3.1 and 7.1fold higher, respectively, than those of the wild type enzyme at pH 7.0 and 70°C in the presence of 1mM Co2+
E410A
-
about 25% of wild-type catalytic efficiency
E458A
-
about 25% of wild-type catalytic efficiency
H411A
-
about 25% of wild-type catalytic efficiency
N433A
-
about 25% of wild-type catalytic efficiency
R373A
-
about 4% of wild-type catalytic efficiency
R408A
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
R408K
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
R472A
-
about 1% of wild-type catalytic efficiency
R479A
-
about 3% of wild-type catalytic efficiency
E410A
-
about 25% of wild-type catalytic efficiency
-
H411A
-
about 25% of wild-type catalytic efficiency
-
R408A
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
-
R408K
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
-
R479A
-
about 3% of wild-type catalytic efficiency
-
E132D
the mutant shows 0.4% activity compared to the wild type enzyme
E67D
the mutant shows 3.7% activity compared to the wild type enzyme
E67Q
the mutant shows 0.8% activity compared to the wild type enzyme
H122Q
the mutant shows 2.0% activity compared to the wild type enzyme
H50Q
the mutant shows 2.0% activity compared to the wild type enzyme
L124A
-
the enzyme shows decreased specific activity for L-ribulose
R142E
-
the enzyme shows decreased specific activity for L-ribulose
R142Q
-
the enzyme shows decreased specific activity for L-ribulose
R142Y
-
the enzyme shows decreased specific activity for L-ribulose
W13F
the mutant shows 41% activity compared to the wild type enzyme
W13H
the mutant shows 52% activity compared to the wild type enzyme
W13Y
the mutant shows 68% activity compared to the wild type enzyme
Y124A
the mutant shows 52% activity compared to the wild type enzyme
E132A
-
the mutants has no activity for L-ribulose; the mutant shows 1.9% activity compared to the wild type enzyme
-
E132D
-
the mutant shows 0.4% activity compared to the wild type enzyme
-